ITA2B_HUMAN - dbPTM
ITA2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITA2B_HUMAN
UniProt AC P08514
Protein Name Integrin alpha-IIb
Gene Name ITGA2B
Organism Homo sapiens (Human).
Sequence Length 1039
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface..
Protein Sequence MARALCPLQALWLLEWVLLLLGPCAAPPAWALNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAPRTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVGSQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTEEAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDFSWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAIAPLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLRSRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAYGANQVAVYRAQPVVKASVQLLVQDSLNPAVKSCVLPQTKTPVSCFNIQMCVGATGHNIPQKLSLNAELQLDRQKPRQGRRVLLLGSQQAGTTLNLDLGGKHSPICHTTMAFLRDEADFRDKLSPIVLSLNVSLPPTEAGMAPAVVLHGDTHVQEQTRIVLDCGEDDVCVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYEAELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVVLCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIRSKNSQNPNSKIVLLDVPVRAEAQVELRGNSFPASLVVAAEEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIHLPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGLPIPSPSPIHPAHHKRDRRQIFLPEPEQPSRLQDPVLVSCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVWTQLLRALEERAIPIWWVLVGVLGGLLLLTILVLAMWKVGFFKRNRPPLEEDDEEGE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
46N-linked_GlycosylationLTFYAGPNGSQFGFS
EEEEECCCCCCEEEE		62.932775232
60PhosphorylationSLDFHKDSHGRVAIV
EEEEEECCCCCEEEE		32.42-
73PhosphorylationIVVGAPRTLGPSQEE
EEEECCCCCCCCCHH		34.7025850435
77PhosphorylationAPRTLGPSQEETGGV
CCCCCCCCCHHCCCE		48.7225850435
81PhosphorylationLGPSQEETGGVFLCP
CCCCCHHCCCEEEEC		38.1825850435
98PhosphorylationAEGGQCPSLLFDLRD
CCCCCCCCEEEECCC		45.3826270265
112PhosphorylationDETRNVGSQTLQTFK
CCCCCCCHHHHHHHH		18.7328060719
181PhosphorylationYSPCRGNTLSRIYVE
CCCCCCCCCEEEEEE		29.0028270605
183PhosphorylationPCRGNTLSRIYVEND
CCCCCCCEEEEEECC		18.0028270605
186PhosphorylationGNTLSRIYVENDFSW
CCCCEEEEEECCCCC		10.7028270605
192PhosphorylationIYVENDFSWDKRYCE
EEEECCCCCCHHHHH		36.9128270605
197PhosphorylationDFSWDKRYCEAGFSS
CCCCCHHHHHHCCCE		10.61-
280N-linked_GlycosylationGEFDGDLNTTEYVVG
EEECCCCCCEEEEEE		50.092775232
319PhosphorylationRGEQMASYFGHSVAV
CHHHHHHHHCCEEEE		12.2118083107
344PhosphorylationLLVGAPLYMESRADR
EEEECCEEECCHHHH		9.5922817900
360PhosphorylationLAEVGRVYLFLQPRG
HHHCCCEEEEECCCC		7.14-
384PhosphorylationLLTGTQLYGRFGSAI
EEECCCEECCCCCCE		9.09-
402PhosphorylationGDLDRDGYNDIAVAA
CCCCCCCCCCEEEEE		17.6028270605
411PhosphorylationDIAVAAPYGGPSGRG
CEEEEECCCCCCCCC		29.9528270605
415PhosphorylationAAPYGGPSGRGQVLV
EECCCCCCCCCEEEE		44.3828270605
427PhosphorylationVLVFLGQSEGLRSRP
EEEEECCCCCCCCCH		31.6527535140
432PhosphorylationGQSEGLRSRPSQVLD
CCCCCCCCCHHHHCC		54.2928270605
435PhosphorylationEGLRSRPSQVLDSPF
CCCCCCHHHHCCCCC		31.6328270605
440PhosphorylationRPSQVLDSPFPTGSA
CHHHHCCCCCCCCCC		25.0328270605
451PhosphorylationTGSAFGFSLRGAVDI
CCCCCCEEEECEECC		19.9624719451
479PhosphorylationGANQVAVYRAQPVVK
CCCEEEEEECCCHHH		7.18-
601N-linked_GlycosylationSPIVLSLNVSLPPTE
CCEEEEEECCCCCCC		20.25UniProtKB CARBOHYD
695PhosphorylationAHYMRALSNVEGFER
HHHHHHHHCCCCHHH		37.5326074081
711N-linked_GlycosylationICNQKKENETRVVLC
HCCCCCCCCCEEEEE		65.892775232
756PhosphorylationSFQLQIRSKNSQNPN
EEEEEEECCCCCCCC		37.5130576142
765UbiquitinationNSQNPNSKIVLLDVP
CCCCCCCEEEEEECC		43.40-
876O-linked_GlycosylationDWGLPIPSPSPIHPA
CCCCCCCCCCCCCCC		38.44-
878O-linked_GlycosylationGLPIPSPSPIHPAHH
CCCCCCCCCCCCCCC		40.60UniProtKB CARBOHYD
891Pyrrolidone_carboxylic_acidHHKRDRRQIFLPEPE
CCCCCCCCCCCCCCC		31.51-
891Pyrrolidone_carboxylic_acidHHKRDRRQIFLPEPE
CCCCCCCCCCCCCCC		31.512226834
891Pyrrolidone_carboxylic_acidHHKRDRRQIFLPEPE
CCCCCCCCCCCCCCC		31.512226834
901PhosphorylationLPEPEQPSRLQDPVL
CCCCCCCCCCCCCEE		45.3730243723
962N-linked_GlycosylationLQSHAWFNVSSLPYA
HHCCCEEECCCCCCC		23.277688323
974PhosphorylationPYAVPPLSLPRGEAQ
CCCCCCCCCCCCHHH		41.9424719451
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseRNF181Q9P0P0
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITA2B_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ITA2B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRB2_HUMANGRB2physical
8631894
THRB_HUMANF2physical
11487023
CO2A1_HUMANCOL2A1physical
7520045
CIB1_HUMANCIB1physical
9030514
PA24A_HUMANPLA2G4Aphysical
18840708
ITB3_HUMANITGB3physical
17032655
ITB3_HUMANITGB3physical
9351872
ITB3_HUMANITGB3physical
11412103
GCN4_YEASTGCN4physical
11412103
ITB3_HUMANITGB3physical
18791937
ITB3_HUMANITGB3physical
10358085
CIB1_HUMANCIB1physical
24163826
FINC_HUMANFN1physical
11478883
FIBG_HUMANFGGphysical
16877710
Drug and Disease Associations
Kegg Disease
H00226 Glanzmann thrombasthenia
OMIM Disease
273800Glanzmann thrombasthenia (GT)
187800Bleeding disorder, platelet-type 16 (BDPLT16)
Kegg Drug
D01029 Tirofiban hydrochloride (USAN); Tirofiban hydrochloride hydrate; Aggrastat (TN)
D02778 Abciximab (genetical recombination) (JAN); Abciximab (USAN/INN); Reopro (TN)
D03971 Elarofiban (USAN)
D04659 Lamifiban (USAN/INN)
D04660 Lamifiban hydrochloride (USAN)
D04785 Lotrafiban hydrochloride (USAN)
D05267 Orbofiban acetate (USAN)
D05772 Roxifiban acetate (USAN)
D05834 Sibrafiban (USAN/INN)
D06335 Xemilofiban hydrochloride (USAN)
D06649 Tadocizumab (USAN)
D06888 Eptifibatide (INN); Integrilin (TN)
D08607 Tirofiban (INN); Agrastat (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITA2B_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-601, AND MASSSPECTROMETRY.
"Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human plateletglycoprotein IIb.";
Calvete J.J., Henschen A., Gonzalez-Rodriguez J.;
Biochem. J. 261:561-568(1989).
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION ATASN-46; ASN-280; ASN-601 AND ASN-711.
O-linked Glycosylation
ReferencePubMed
"Localization of an O-glycosylation site in the alpha-subunit of thehuman platelet integrin GPIIb/IIIa involved in Baka (HPA-3a)alloantigen expression.";
Calvete J.J., Muniz-Diaz E.;
FEBS Lett. 328:30-34(1993).
Cited for: PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT SER-878.

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